The rational development of new antineoplastic agents directed against tubulin, a protein critical for cell division, requires greater understanding of the interaction between the polypeptide subunits of tubulin, its two tightly bound guanine nucleotides, and microtubule-associated proteins (MAPS). The effects of nucleotides on the stability of microtubules continued to be examined, as were conditions to optimize the separation of alpha-tubulin and beta-tubulin on a preparative scale. The purification of a microtubule-associated protein which causes the formation of microtubule bundles continued to progress, and a project to introduce potentially antimitotic nucleotide analogs into cells continued. Studies with 1-thiophosphate analogs of GDP, GTP, 2',3'-dideoxyguanosine nucleotides were begun. A project to localize the nonexchangeable GTP binding site was continued.